Identification of amidicin: a novel peptide with C-terminal amide structure isolated from porcine cardiac atrium
| Autor: | Yuichiro Ishiyama, Kazuo Kitamura, Tanenao Eto |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Pituitary gland
Swine Biophysics Ethyl acetate Peptide Biochemistry chemistry.chemical_compound Amide medicine Animals Tissue Distribution Amino Acid Sequence Heart Atria Molecular Biology Peptide sequence chemistry.chemical_classification biology Cardiac Ventricle Radioimmunoassay Cell Biology Amides medicine.anatomical_structure chemistry biology.protein Antibody Peptides |
| Zdroj: | Biochemical and Biophysical Research Communications. 293:741-746 |
| ISSN: | 0006-291X |
| Popis: | Using a novel method employing a V8 protease digestion coupled with ethyl acetate extraction, we have purified a peptide with C-terminal amide structure from porcine cardiac atrium. The peptide was determined to be Ala-Val-Leu-Gly-Leu-CONH2. According to the sequence, we have raised an antibody and established the radioimmunoassay. Using this radioimmunoassay, we have isolated a novel 14 amino acid peptide where C-terminus was amidated. This peptide was termed amidicin. Amidicin is widely distributed in porcine tissue and is especially abundant in pituitary gland, cardiac ventricle, and spleen. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect